ArticleBiophysical journal2005
Coarse-grained strategy for modeling protein stability in concentrated solutions.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Contrasting the Influence of Cationic Amino Acids on the Viscosity and Stability of a Highly Concentrated Monoclonal Antibody.Pharmaceutical research · 2017Article
- Reaching new levels of realism in modeling biological macromolecules in cellular environments.Journal of molecular graphics & modelling · 2013Review
- Article
- Competition between folding and aggregation in a model for protein solutions.The European physical journal. E, Soft matter · 2010Article
- Structure and thermodynamics of colloidal protein cluster formation: comparison of square-well and simple dipolar models.The Journal of chemical physics · 2009Article
- Thermodynamics and kinetics of protein folding under confinement.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Influence of macromolecular crowding on protein-protein association rates--a Brownian dynamics study.Biophysical journal · 2008Article
- Coarse-grained strategy for modeling protein stability in concentrated solutions. III: directional protein interactions.Biophysical journal · 2007Article
- Heteropolymer collapse theory for protein folding in the pressure-temperature plane.Biophysical journal · 2006Article
- Coarse-grained strategy for modeling protein stability in concentrated solutions. II: phase behavior.Biophysical journal · 2006Article
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2 authors.
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Abstract
We present a coarse-grained approach for modeling the thermodynamic stability of single-domain globular proteins in concentrated aqueous solutions. Our treatment derives effective protein-protein interactions from basic structural and energetic characteristics of the native and denatured states. These characteristics, along with the intrinsic (i.e., infinite dilution) thermodynamics of folding, are calculated from elementary sequence information using a heteropolymer collapse theory. We integrate this information into Reactive Canonical Monte Carlo simulations to investigate the connections between protein sequence hydrophobicity, protein-protein interactions, protein concentration, and the thermodynamic stability of the native state. The model predicts that sequence hydrophobicity can affect how protein concentration impacts native-state stability in solution. In particular, low hydrophobicity proteins are primarily stabilized by increases in protein concentration, whereas high hydrophobicity proteins exhibit richer nonmonotonic behavior. These trends appear qualitatively consistent with the available experimental data. Although factors such as pH, salt concentration, and protein charge are also important for protein stability, our analysis suggests that some of the nontrivial experimental trends may be driven by a competition between destabilizing hydrophobic protein-protein attractions and entropic crowding effects.
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